Purification and characterization of a lactonase from Burkholderia sp R-711, that hydrolyzes (R)-5-oxo-2-tetrahydrofurancarboxylic acid

Authors
Citation
K. Mochizuki, Purification and characterization of a lactonase from Burkholderia sp R-711, that hydrolyzes (R)-5-oxo-2-tetrahydrofurancarboxylic acid, ARCH MICROB, 175(6), 2001, pp. 430-434
Citations number
16
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
ARCHIVES OF MICROBIOLOGY
ISSN journal
0302-8933 → ACNP
Volume
175
Issue
6
Year of publication
2001
Pages
430 - 434
Database
ISI
SICI code
0302-8933(200106)175:6<430:PACOAL>2.0.ZU;2-3
Abstract
A lactonase hydrolyzing (R)-5-oxo-2-tetrahydrofurancarboxylic acid to D-alp ha -hydroxyglutaric acid was purified 170-fold with 2% recovery to near hom ogeneity from crude extracts of Burkholderia sp. R-711, which had been isol ated as a bacterium able to assimilate (R)-5-oxo-2-tetrahydrofurancarboxyli c acid. The molecular mass was estimated to be 33 kDa by gel filtration. Th e purified preparation migrated as a single band of molecular mass 38 kDa u pon SDS-PAGE. The maximum activity was observed at pH 7.0-8.0 and 35-40 deg reesC. The enzyme required no added cofactors or metal ions: the activity w as inhibited to 60-100% by SH-blocking reagents, but was not affected by me tal-chelating reagents. The enzyme showed lower activity and affinity towar d (S)-5-oxo-2-tetrahydrofurancarboxylic acid, but did not act on other natu ral and synthetic lactones tested.